Background. The hydrogenosomes of the anaerobic ciliate Nyctotherus ovalis show how mitochondria can evolve into hydrogenosomes because they possess a mitochondrial genome and parts of an electron-transport chain on the one hand, and a hydrogenase on the other hand. The hydrogenase permits direct reoxidation of NADH because it consists of a [FeFe] hydrogenase module that is fused to two modules, which are homologous to the 24 kDa and the 51 kDa subunits of a mitochondrial complex I. Results. The [FeFe] hydrogenase belongs to a clade of hydrogenases that are different from well-known eukaryotic hydrogenases. The 24 kDa and the 51 kDa modules are most closely related to homologous modules that function in bacterial [NiFe] hydrogenases. Paralogous, mitochondrial 24 kDa and 51 kDa modules function in the mitochondrial complex I in N. ovalis. The different hydrogenase modules have been fused to form a polyprotein that is targeted into the hydrogenosome. Conclusion. The hydrogenase and their associated modules have most likely been acquired by independent lateral gene transfer from different sources. This scenario for a concerted lateral gene transfer is in agreement with the evolution of the hydrogenosome from a genuine ciliate mitochondrion by evolutionary tinkering. © 2007 Boxma et al; licensee BioMed Central Ltd.
CITATION STYLE
Boxma, B., Ricard, G., Van Hoek, A. H. A. M., Severing, E., Moon-Van Der Staay, S. Y., Van Der Staay, G. W. M., … Hackstein, J. H. P. (2007). The [FeFe] hydrogenase of Nyctotherus ovalis has a chimeric origin. BMC Evolutionary Biology, 7(1). https://doi.org/10.1186/1471-2148-7-230
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